Alkene/Alkane-Bridged Mimics of the Lantibiotic Nisin: Toward Novel Peptide-Based Antibiotics
Nisin belongs to a class of natural antimicrobial peptides, the lantibiotics, which is produced by a broad range of bacteria e.g. Bacillus, Lactococcus, Streptomyces and Staphylococcus species . A general feature of these peptides is the presence of a lanthionine moiety (thioether- or sulfide bridge) which gives these peptides their specific bioactive conformation.
Nisin binds with its N-terminus to lipid II thereby enabling the C-terminus to form pores in the phospholipid membrane which ultimately leads to cell leakage and causes a collapse of the vital ion gradients across the cell membrane. Lipid II is an important target for many antimicrobial peptides such as vancomycin, ramoplanin and nisin and serves as a general target for the development of new antibiotics .
KeywordsAntimicrobial Peptide Large Unilamellar Vesicle Bioactive Conformation Covalent Constraint Terminal Alkene